Magainin 2 in phospholipid bilayers:: peptide orientation and lipid chain ordering studied by X-ray diffraction

被引:39
作者
Münster, C
Spaar, A
Bechinger, B
Salditt, T
机构
[1] Univ Saarland, D-66041 Saarbrucken, Germany
[2] Univ Strasbourg 1, Inst Le Bel, F-67000 Strasbourg, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2002年 / 1562卷 / 1-2期
关键词
X-ray diffraction; antibiotic peptide; lipid-peptide interaction;
D O I
10.1016/S0005-2736(02)00357-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We present a structural study of biomimetic lipid bilayers interacting with the antimicrobial peptide magainin 2 amide, using grazing incidence X-ray diffraction and reciprocal space mapping (RSM) techniques. The short-range order of lipid chains in lecithin is found to be strongly reduced by the peptides. From the scattering intensity of the chain correlation peak, we can quantify the lateral length scale R over which the bilayer structure is affected by peptide binding. The non-local perturbation of the bilayer is discussed in the framework of bilayer elasticity theory. (C) 2002 Elsevier Science B.V. All tights reserved.
引用
收藏
页码:37 / 44
页数:8
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